Protein-polymer colloids are of recent interest from fundamental point of view as well as due to their high promise for biological applications such as biocatalysis, imaging, cancer drug delivery. Here, we examined the peroxidase activities of cytochrome c-poly(acrylic acid) (cyt c-PAA) covalent conjugates where the molecular weight of PAA has been increased systematically. A linear relation between the enzymatic activity and molecular weight of the PAA was observed, and up to 17-fold enhancement in turnover number (kcat) was noted. The colloids of cyt c-PAA were characterized by dynamic light scattering, electron microscopy and other biophysical methods. The effects of macromolecular crowding, substrate partitioning in the polymer phase, and PAA negative charge field on the kinetic enhancement were systematically studied. Taken together, these data indicated that polymer charge density and macromolecular crowding by the conjugated polymer could be adjusted to enhance the redox activity of cyt c. This concept was then extended to build colloids of horseradish peroxidase and hemoglobin, as well as enzyme-polymer films. Full biochemical and biophysical characterization will be presented.

Protein-polymer colloids: 17-fold enhanced activities of cytochrome c conjugated with poly(acrylic acid)

256th National Meeting (2018)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.